Homologous Recombination (HR) is an evolutionarily conserved error-free pathway for repairing DNA. This pathway is a highly regulated reaction initiated by a double strand break within the genome. A host of proteins play vital roles within HR, including the RecA-like family of DNA recombinases. Members of this family of proteins are DNA-dependent ATPases that catalyze the central reactions of HR. To accomplish these functions, RecA and its eukaryotic homolog Rad51 bind to single stranded DNA (ssDNA). Crucial to this role is the need for ATP binding in order to form an extended nucleoprotein filament in complex with ssDNA. This binding results in the DNA increasing in length and generating a complex competent for strand invasion. Once the reaction is complete, the recombinase must be removed from double stranded DNA (dsDNA) for subsequent steps in HR. Using single molecule techniques, the interaction between DNA and Rad51 from both human and Saccharomyces cerevisiae is investigated including the role of nucleotide binding, ATP hydrolysis, and mediators. The results increase the understanding of the fundamental molecular mechanisms underlying the HR pathway.
|School Location:||United States -- New York|
|Source:||DAI-B 70/02, Dissertation Abstracts International|
|Subjects:||Molecular biology, Biochemistry, Biophysics|
|Keywords:||DNA damage, Fluorescence, Homologous recombination, Rad51, Single-molecule, TIRF|
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